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Mitochondrial Rieske iron-sulfur protein in pulmonary artery smooth muscle: A key primary signaling molecule in pulmonary hypertension
- Truong, Lillian, Zheng, Yun-Min, Wang, Yong-Xiao
- Archives of biochemistry and biophysics 2019 v.664 pp. 68-75
- NAD(P)H oxidase (H2O2-forming), NADP (coenzyme), death, electron transport chain, heart failure, hypertension, mitochondria, protein kinase C, protein subunits, pulmonary artery, reactive oxygen species, ryanodine receptors, signal transduction, smooth muscle, vasoconstriction
- Rieske iron-sulfur protein (RISP) is a catalytic subunit of the complex III in the mitochondrial electron transport chain. Studies for years have revealed that RISP is essential for the generation of intracellular reactive oxygen species (ROS) via delicate signaling pathways associated with many important molecules such as protein kinase C-ε, NADPH oxidase, and ryanodine receptors. More significantly, mitochondrial RISP-mediated ROS production has been implicated in the development of hypoxic pulmonary vasoconstriction, leading to pulmonary hypertension, right heart failure, and death. Investigations have also shown the involvement of RISP in ROS-dependent cardiac ischemic/reperfusion injuries. Further research may provide novel and valuable information that can not only enhance our understanding of the functional roles of RISP and the underlying molecular mechanisms in the pulmonary vasculature and other systems, but also elucidate whether RISP targeting can act as preventative and restorative therapies against pulmonary hypertension, cardiac diseases, and other disorders.